COP6_COPC7
ID COP6_COPC7 Reviewed; 325 AA.
AC A8NCK5;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Alpha-cuprenene synthase COP6 {ECO:0000303|PubMed:19400802};
DE EC=4.2.3.- {ECO:0000269|PubMed:19400802, ECO:0000269|PubMed:20419721};
DE AltName: Full=Sesquiterpene synthase COP6 {ECO:0000303|PubMed:19400802};
GN Name=COP6 {ECO:0000303|PubMed:19400802}; ORFNames=CC1G_03563;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19400802; DOI=10.1111/j.1365-2958.2009.06717.x;
RA Agger S., Lopez-Gallego F., Schmidt-Dannert C.;
RT "Diversity of sesquiterpene synthases in the basidiomycete Coprinus
RT cinereus.";
RL Mol. Microbiol. 72:1181-1195(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20419721; DOI=10.1002/cbic.200900671;
RA Lopez-Gallego F., Agger S.A., Abate-Pella D., Distefano M.D.,
RA Schmidt-Dannert C.;
RT "Sesquiterpene synthases Cop4 and Cop6 from Coprinus cinereus: catalytic
RT promiscuity and cyclization of farnesyl pyrophosphate geometric isomers.";
RL ChemBioChem 11:1093-1106(2010).
CC -!- FUNCTION: Alpha-cuprenene synthase; part of the gene cluster that
CC mediates the biosynthesis of alpha-cuprenene and oxidized derivatives
CC (PubMed:19400802). The alpha-cuprenene synthase COP6 is the only
CC sesquiterpene synthase identified in C.cinereus that appears to be part
CC of a biosynthetic gene cluster and is highly specific since it
CC catalyzes the cyclization of (2E,6E)-farnesyl diphosphate into only one
CC product, alpha-cuprenene (PubMed:19400802, PubMed:20419721). COP6 is
CC also able to perform the cyclization of geranyl diphosphate
CC (PubMed:20419721). The cytochrome P450 monooxygenase COX2 then oxidizes
CC the cyclohexadiene ring of alpha-cuprenene at positions 1 and 4,
CC yielding first alpha-cuparene, followed by alpha-cuparophenol and a
CC further yet unidentified compound resulting from one additional
CC oxidation step (PubMed:19400802). The cytochrome P450 monooxygenase
CC COX1 then likely catalyzes the oxidation at position 9 of the pentane
CC ring of alpha-cuprenene to give the corresponding hydroxy or ketone
CC derivatives (PubMed:19400802). {ECO:0000269|PubMed:19400802,
CC ECO:0000269|PubMed:20419721}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P13513};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.6 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:20419721};
CC KM=1.5 uM for geranyl diphosphate {ECO:0000269|PubMed:20419721};
CC -!- SIMILARITY: Belongs to the trichodiene synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACS02000009; EAU89298.1; -; Genomic_DNA.
DR RefSeq; XP_001832549.1; XM_001832497.1.
DR AlphaFoldDB; A8NCK5; -.
DR SMR; A8NCK5; -.
DR STRING; 240176.A8NCK5; -.
DR EnsemblFungi; EAU89298; EAU89298; CC1G_03563.
DR GeneID; 6009036; -.
DR KEGG; cci:CC1G_03563; -.
DR VEuPathDB; FungiDB:CC1G_03563; -.
DR eggNOG; ENOG502SQ3X; Eukaryota.
DR InParanoid; A8NCK5; -.
DR OMA; CHSTIIK; -.
DR OrthoDB; 1430313at2759; -.
DR SABIO-RK; A8NCK5; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR024652; Trichodiene_synth.
DR Pfam; PF06330; TRI5; 1.
DR SFLD; SFLDG01021; Trichodiene_Synthase_Like; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..325
FT /note="Alpha-cuprenene synthase COP6"
FT /id="PRO_0000444636"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
SQ SEQUENCE 325 AA; 37424 MW; 75E07825E870D5A7 CRC64;
MPAALPYNVS RDNKWDIKKI IQDFFKRCDV PYQVIPYDTE LWNACLKRAK EKGYPVEPDS
PMSLYRSFKV GVVITRTSYG HIQDYEILIW VATFTAFVTY ADDAFQEDIQ HLHSFARTFL
QNEKHEHPVL EAFAQFLRES SIRFSHFVAN TVVSSALRFM MSIALEFEGQ NVSVSTEARE
YPGYIRILSG LSDIYALFAF PMDLPRSTYI QAFPEQIDYI NGTNDLLSFY KEELDCETVN
FISAAATSQQ VSKLEVLRNA AEKAAYSYDV VVNVLKPYPE ALAAWKSFAR GFCYFHTSSP
RYRLGEMFHD FEHDLVCKCA SCTEI
